Section Editors

  • James Chou, Harvard Medical School
  • Jianping Ding, Shanghai Institutes of Biological Sciences
  • Jean-Luc Pellequer, CEA Marcoule
  • Paul A Ramsland, Macfarlane Burnet Institute for Medical Research and Public Health
  • Torsten Schwede, Biozentrum Univ. of Basel, SIB Swiss Institute of Bioinformatics

Executive Editor

  • Simon Harold, BioMed Central

Articles

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  • Image attributed to: Fig 2 Barros et al BMC Structural Biology

    Major structural role for PHP domain

    Metal binding can be restored to E. coli polymerase III PHP domain with only three point mutations, demonstrating that the domain structure is highly conserved and is a major structural element of this bacterial replicative polymerase.

    BMC Structural Biology 2013, 13:8
  • Image attributed to: Fig 4 Gana et al BMC Structural Biology 2013 13,6

    Ligand-centric protein annotation

    A new systematic approach for grouping protein structures based upon the type and conformation of the ligand they bind to reveals some unexpected findings and extends the existing structural classification of S-adenosyl-L-13 methionine (SAM) binding proteins

    BMC Structural Biology 2013, 13:6
  • Image attributed to: Fig 2A Olivella et al BMC Structural Biology 2013 13,3

    Unique role for Cys6.47 in class A GPCRs

    Analysis of G protein-coupled receptor (GPCR) crystal structures and molecular dynamics simulations of model peptides suggests Cys6.47 is the gate keeper of a hydrogen bond network involving residues known to be crucial to receptor activation.

    BMC Structural Biology 2013, 13:3
  • Image attributed to: Fig 4A Park et al BMC Struc Bio 2012 12,32

    Conformational changes in FPPS complex

    Three crystal structures of human farnesyl pyrophosphate synthase (FPPS) in ternary complex with a novel bisphosphonate inhibitor reveal mechanistic insight of the conformational change in the C-terminal tail closure that is essential for catalysis.

    BMC Structural Biology 2012, 12:32
  • Image attributed to: Fig 7 Smith et al BMC Struct Bio (2012) 12,31

    Modeling macromolecules with nano-objects

    Protein Nano-Object Integrator (ProNOI) is a novel software tool for generating atomic-style nano shapes in conjunction with biological macromolecules, allowing users to manipulate shape, dimension and position, and charge objects with user-specified charge density.

    BMC Structural Biology 2012, 12:31
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Scope

BMC Structural Biology is an open access, peer-reviewed journal that considers articles on investigations into the structure of biological macromolecules, including solving structures, structural and functional analyses, and computational modeling.

It is journal policy to publish work deemed by peer reviewers to be a coherent and sound addition to scientific knowledge and to put less emphasis on interest levels, provided that the research constitutes a useful contribution to the field.

Section Editor's profile

Dr Ramsland

Dr Ramsland is currently the Sir Zelman Cowen Fellow and a Group Leader in the Centre for Immunology at the Burnet Institute (Melbourne, Australia). His research examines the diverse structural roles of carbohydrates and glycoproteins in immunity and infection (Structural Glycobiology) using crystallography, computational modelling, automated docking and solution scattering techniques. He has over 90 scientific publications including primary research papers, reviews/chapters and has recently co-edited a book on Structural Glycobiology.

"Together with Dr Cy Jeffries, Deputy Section Editor, I am pleased to be involved in guiding the development of the Small-Angle Scattering section of BMC Structural Biology. This new section incorporates all aspects of the structural analysis of biological macromolecules using techniques in small-angle scattering including but not limited to: studies incorporating substantial analysis by small-angle X-ray scattering and/or neutron scattering."

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ISSN: 1472-6807